Carbohydrates are involved in many important biological processes. Natural polysaccharides are often able to perform complex functions via well-controlled multivalent interactions of key functional motifs with corresponding binding proteins. To date, there have been many attempts to design glycomimetics that are capable of recapitulating some of these binding events that take place in nature.
While some structural guidelines to the design of glycomimetics are available, precise control of the polymer backbone conformations of these glycomimetics is still lacking. This has hampered efforts to understand or mimic the binding of these natural polysaccharides to their binding molecules. Studies with α-helical glycopeptides, for example, have revealed that the variation in α-helicities of these glycopeptides stem from relatively low thermodynamic stabilities, pendant group dependencies and complementary interactions with proteins. This makes it particularly difficult to design binding or functional motifs at desired positions on glycomimetics to facilitate binding to their corresponding binding molecules.
There is a need to provide glycomimetics that overcome, or at least ameliorate, one or more of the disadvantages described above.
There is a need to provide glycomimetics that not only maintain key properties of natural polysaccharides, but also adopt a predictable, well-defined and stable conformation that enable binding or functional motifs to be more accurately and optimally positioned on its backbone and therefore, improved control of their multivalent interactions with binding molecules.